Component

Hercynine / N-alpha-trimethylhistidine

Context-specific entity; species, compartment and exposure are stated on each claim.

8 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What acts on it

  1. Reconstituted Mycobacterium smegmatis biosynthesis required an iron(II)-dependent oxidative sulfurization step.

    Mycobacterium smegmatis EgtB → Hercynine / N-alpha-trimethylhistidine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified bacterial pathway.
    limitations
    Does not mean iron supplements increase human synthesis.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    Iron supports a microbial synthesis enzyme.
    primary_references
    In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20420449/ · DOI 10.1021/ja101721e

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 176–182

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified bacterial pathway. · source_derived_draft · unverified_draft

    ## ergothioneine-bacterial-iron-step Iron supports a microbial synthesis enzyme. Reconstituted Mycobacterium smegmatis biosynthesis required an iron(II)-dependent oxidative sulfurization step. Model: Purified bacterial pathway. Limitations: Does not mean iron supplements increase human synthesis. Evidence access: Primary abstract In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20420449/ · DOI 10.1021/ja101721e
    Complete structured claim and evidence

  2. Structural and kinetic analyses of Chlorobium limicola EanB supported sulfurization of hercynine in anaerobic ergothioneine synthesis.

    Chlorobium limicola EanB → Hercynine / N-alpha-trimethylhistidine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Bacterial enzyme crystal structure and kinetics.
    limitations
    Do not project this microbial enzyme onto human tissues.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    Different machinery can produce the same compound.
    primary_references
    Structural and Mechanistic Basis for Anaerobic Ergothioneine Biosynthesis. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30943021/ · DOI 10.1021/jacs.8b12596

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 224–230

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Bacterial enzyme crystal structure and kinetics. · source_derived_draft · unverified_draft

    ## ergothioneine-eanb-mechanism Different machinery can produce the same compound. Structural and kinetic analyses of Chlorobium limicola EanB supported sulfurization of hercynine in anaerobic ergothioneine synthesis. Model: Bacterial enzyme crystal structure and kinetics. Limitations: Do not project this microbial enzyme onto human tissues. Evidence access: Primary abstract Structural and Mechanistic Basis for Anaerobic Ergothioneine Biosynthesis. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30943021/ · DOI 10.1021/jacs.8b12596
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Chlorobium limicola enzymes synthesized ergothioneine without oxygen through a rhodanese-like sulfur-transfer route.

    Chlorobium limicola EanB → L-Ergothioneine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Enzymes from a strictly anaerobic green sulfur bacterium.
    limitations
    Anaerobic production does not establish a non-antioxidant function in humans.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    An alternative microbial route does not need oxygen.
    primary_references
    Anaerobic Origin of Ergothioneine. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28786519/ · DOI 10.1002/anie.201705932

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 216–222

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Enzymes from a strictly anaerobic green sulfur bacterium. · source_derived_draft · unverified_draft

    ## ergothioneine-anaerobic-synthesis An alternative microbial route does not need oxygen. Chlorobium limicola enzymes synthesized ergothioneine without oxygen through a rhodanese-like sulfur-transfer route. Model: Enzymes from a strictly anaerobic green sulfur bacterium. Limitations: Anaerobic production does not establish a non-antioxidant function in humans. Evidence access: Primary abstract Anaerobic Origin of Ergothioneine. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28786519/ · DOI 10.1002/anie.201705932
    Complete structured claim and evidence

  2. Mycobacterium thermoresistibile EgtB coupled gamma-glutamylcysteine to hercynine through an oxygen-dependent C-S bond-forming reaction.

    Mycobacterium thermoresistibile EgtB → Gamma-glutamylcysteine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Crystal structure and enzyme mechanism study.
    limitations
    Non-heme iron coordination supports a proposed radical mechanism, not direct observation of every intermediate.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    A cysteine-containing precursor supplies sulfur.
    primary_references
    Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25597398/ · DOI 10.1002/anie.201410045

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 184–190

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Crystal structure and enzyme mechanism study. · source_derived_draft · unverified_draft

    ## ergothioneine-egtb-sulfur-donor A cysteine-containing precursor supplies sulfur. Mycobacterium thermoresistibile EgtB coupled gamma-glutamylcysteine to hercynine through an oxygen-dependent C-S bond-forming reaction. Model: Crystal structure and enzyme mechanism study. Limitations: Non-heme iron coordination supports a proposed radical mechanism, not direct observation of every intermediate. Evidence access: Primary abstract Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25597398/ · DOI 10.1002/anie.201410045
    Complete structured claim and evidence

  3. Mycobacterium smegmatis EgtD uses SAM-dependent methyl transfer to convert histidine into hercynine.

    S-Adenosyl-L-methionine → Mycobacterium smegmatis EgtD source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Apo and ligand-bound enzyme structures.
    limitations
    No evidence that human ergothioneine consumption drains SAM; humans lack this established synthesis pathway.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    The microbial synthesis branch connects to methyl-donor chemistry.
    primary_references
    Structural insights into the histidine trimethylation activity of EgtD from Mycobacterium smegmatis. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25251321/ · DOI 10.1016/j.bbrc.2014.09.058

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 552–558

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Apo and ligand-bound enzyme structures. · source_derived_draft · unverified_draft

    ## ergothioneine-egtd-sam The microbial synthesis branch connects to methyl-donor chemistry. Mycobacterium smegmatis EgtD uses SAM-dependent methyl transfer to convert histidine into hercynine. Model: Apo and ligand-bound enzyme structures. Limitations: No evidence that human ergothioneine consumption drains SAM; humans lack this established synthesis pathway. Evidence access: Primary abstract Structural insights into the histidine trimethylation activity of EgtD from Mycobacterium smegmatis. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25251321/ · DOI 10.1016/j.bbrc.2014.09.058
    Complete structured claim and evidence

  4. Reconstituted Mycobacterium smegmatis biosynthesis used a methyltransferase to add three methyl groups to the histidine alpha-amino group, producing hercynine.

    Mycobacterium smegmatis EgtD → L-Histidine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant bacterial enzyme pathway.
    limitations
    Humans have no established equivalent ergothioneine biosynthetic pathway.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    Microbes first modify histidine before adding sulfur.
    primary_references
    In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20420449/ · DOI 10.1021/ja101721e

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 168–174

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant bacterial enzyme pathway. · source_derived_draft · unverified_draft

    ## ergothioneine-histidine-methylation Microbes first modify histidine before adding sulfur. Reconstituted Mycobacterium smegmatis biosynthesis used a methyltransferase to add three methyl groups to the histidine alpha-amino group, producing hercynine. Model: Recombinant bacterial enzyme pathway. Limitations: Humans have no established equivalent ergothioneine biosynthetic pathway. Evidence access: Primary abstract In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20420449/ · DOI 10.1021/ja101721e
    Complete structured claim and evidence

  5. Human whole-blood ergothioneine correlated with hercynine and S-methyl-ergothioneine, consistent with possible metabolism.

    Human blood ergothioneine concentration, compartment specified → S-Methyl-ergothioneine source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human oral-administration study.
    limitations
    Correlation does not identify the human enzymes or prove every conversion direction.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    Related molecules may help trace its fate.
    primary_references
    Administration of Pure Ergothioneine to Healthy Human Subjects: Uptake, Metabolism, and Effects on Biomarkers of Oxidative Damage and Inflammation. · 2017 · https://pubmed.ncbi.nlm.nih.gov/27488221/ · DOI 10.1089/ars.2016.6778
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 472–478

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human oral-administration study. · source_derived_draft · unverified_draft

    ## ergothioneine-human-metabolite-markers Related molecules may help trace its fate. Human whole-blood ergothioneine correlated with hercynine and S-methyl-ergothioneine, consistent with possible metabolism. Model: Human oral-administration study. Limitations: Correlation does not identify the human enzymes or prove every conversion direction. Evidence access: Primary abstract Administration of Pure Ergothioneine to Healthy Human Subjects: Uptake, Metabolism, and Effects on Biomarkers of Oxidative Damage and Inflammation. · 2017 · https://pubmed.ncbi.nlm.nih.gov/27488221/ · DOI 10.1089/ars.2016.6778
    Complete structured claim and evidence

  6. At pH 7.4, ergothioneine and hercynine generated different products after chemically generated singlet oxygen exposure.

    L-Ergothioneine → Singlet molecular oxygen source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    LC-MS analysis with a thermal singlet-oxygen donor.
    limitations
    Product-based reaction model; not proof that this is its exclusive physiological function.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    The sulfur atom changes the reaction route.
    primary_references
    Ergothioneine stands out from hercynine in the reaction with singlet oxygen: Resistance to glutathione and TRIS in the generation of specific products indicates high reactivity. · 2017 · https://pubmed.ncbi.nlm.nih.gov/29074402/ · DOI 10.1016/j.freeradbiomed.2017.10.372

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 136–142

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · LC-MS analysis with a thermal singlet-oxygen donor. · source_derived_draft · unverified_draft

    ## ergothioneine-singlet-oxygen The sulfur atom changes the reaction route. At pH 7.4, ergothioneine and hercynine generated different products after chemically generated singlet oxygen exposure. Model: LC-MS analysis with a thermal singlet-oxygen donor. Limitations: Product-based reaction model; not proof that this is its exclusive physiological function. Evidence access: Primary abstract Ergothioneine stands out from hercynine in the reaction with singlet oxygen: Resistance to glutathione and TRIS in the generation of specific products indicates high reactivity. · 2017 · https://pubmed.ncbi.nlm.nih.gov/29074402/ · DOI 10.1016/j.freeradbiomed.2017.10.372
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

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